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Q02PQ1 (NADK_PSEAB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD kinase

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase
Gene names
Name:nadK
Ordered Locus Names:PA14_24220
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]
Taxonomic identifier208963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP By similarity. HAMAP-Rule MF_00361

Catalytic activity

ATP + NAD+ = ADP + NADP+. HAMAP-Rule MF_00361

Cofactor

Divalent metal ions By similarity. HAMAP-Rule MF_00361

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processNAD metabolic process

Inferred from electronic annotation. Source: InterPro

NADP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295NAD kinase HAMAP-Rule MF_00361
PRO_1000005429

Regions

Nucleotide binding72 – 732NAD By similarity
Nucleotide binding146 – 1472NAD By similarity
Nucleotide binding187 – 1926NAD By similarity

Sites

Active site721Proton acceptor By similarity
Binding site1571NAD By similarity
Binding site1741NAD By similarity
Binding site1761NAD By similarity
Binding site2471NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02PQ1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 2567446028BAA419

FASTA29532,140
        10         20         30         40         50         60 
MEPFRNIGII GRLGSTQVLD TIRRLKKFLI DRHLHVILED TIAEVLPGHG LQTCSRKIMG 

        70         80         90        100        110        120 
EICDLVVVVG GDGSMLGAAR ALARHKVPVL GINRGSLGFL TDIRPDELEA KVGEVLDGQY 

       130        140        150        160        170        180 
IVESRFLLDA QVRRGIDSMG QGDALNDVVL HPGKSTRMIE FELYIDGQFV CSQKADGLIV 

       190        200        210        220        230        240 
ATPTGSTAYA LSAGGPIMHP KLDAIVIVPM YPHMLSSRPI VVDGNSELKI VVSPNMQIYP 

       250        260        270        280        290 
QVSCDGQNHF TCAPGDTVTI SKKPQKLRLI HPIDHNYYEI CRTKLGWGSR LGGGD 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ12320.1.
RefSeqYP_790085.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02PQ1.
SMRQ02PQ1. Positions 4-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_24220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ12320; ABJ12320; PA14_24220.
GeneID4384119.
KEGGpau:PA14_24220.
PATRIC19850001. VBIPseAer79785_1961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycPAER208963:GI5K-1958-MONOMER.

Family and domain databases

Gene3D2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPMF_00361. NAD_kinase.
InterProIPR017438. ATP-NAD_kinase_dom_1.
IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
IPR002504. PolyP/ATP_NADK.
[Graphical view]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADK_PSEAB
AccessionPrimary (citable) accession number: Q02PQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families